2.To the right is a schematic diagram ofHis $7the active site in the Michaelis complex of a-chy-motrypsin and a polypeptide substrate. Describebriefly the catalytic or structural roles of theresidues listed below:но — Ser195(а) Ser195AA,-C-ÇH-NH-C-ÇH -NH -AAnRRHH.193GlySer195(b) His57(c) NH groups of Gly193 and Ser195(d) The most favorable side chain R for binding(e) Identify the scissile bond with an arrow, i.e., the bond in the peptide substrate that is cleaved as aresult of the catalytic action of the enzyme. You can point to it on the diagram above.

Chymotrypsin is a protease that cleaves a peptide at the C-terminal of aromatic amino acids like…

To the right is a schematic diagram of site in the Michaelis complex of a-chy- motrypsin and a polypeptide substrate. Describe briefly the catalytic or structural roles of the residues listed below: 2. the active (a) Ser195 (b) His57 (c) NH groups of Gly193 and Ser195 (d) The most favorable side chain R for binding (e) Identify the scissile bond with an arrow, i.e., the

To the right is a schematic diagram of site in the Michaelis complex of a-chy- motrypsin and a polypeptide substrate. Describe briefly the catalytic or structural roles of the residues listed below: 2. the active (a) Ser195 (b) His57 (c) NH groups of Gly193 and Ser195 (d) The most favorable side chain R for binding (e) Identify the scissile bond with an arrow, i.e., the

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 8TYK: Which of the following statements about the allosteric site is true? a. The allosteric site is a...

See similar textbooks

Similar questions

Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
1 ).Which of the following accurately describes substrate specificity for serine proteases? A.The binding cleft B.Mg2+ metal activated enzyme C.The catalytic triad D.Facilitates redox chemistry E.Stabilizes the transition state 2). Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? select all that apply leucine aspartic acid histidine lysine Please answer both correct i will give u upvote.
#1)What are the main roles of the following amino acids; (within the crystal structure and/or active site. be specific, with pictures and mechanistic arrows as needed) -Glu305 from pyruvate carboxylase -Gln23 from Penecilin Acylase -Ser203 from Acetylcholinesterase #2) Why is L-tetrahydro-2-furoic acid would be a suitable inhibitor for Proline oxidase?
#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)
1. Depict the structure features in the active site of cysteine protease 2. provide a step-wise reaction mechanism to show the hydrolysis of the peptide bond catalyzed by a cysteine protease
8. Match each of the following amino acids with the intermediate needed for its synthesis.(a) 3-Phosphoglycerate 1. glutamate 2. serine 3. asparagine (b) oxaloacetate 1. glutamate 2. serine 3. Asparagine
2. A mixture of the following amino acids (glu, leu, val, arg, ser, phe) was obtained upon complete hydrolysis of a hexapeptide. a. Edman’s reagent releases leucine b. Hexapeptide with carboxypeptidase releases serine. c. Hexapeptide with trypsin forms a tripeptide A with leucine at the N terminal and tripeptide B with valine at the N terminal. d. Tripeptide A with carboxypeptidase releases arginine and a dipeptide with glutamic acid at C terminal. e. Tripeptide B with chymotrypsin form releases serine and another dipeptide. Give: 1. the amino acid sequence of tripeptide A and B. 2. the amino acid sequence in the above hexapeptide.
9) Considering the enzymatic reaction catalyzed by HIV protease: Options A) hydrolysis is the net reaction observed. B) a peptide bond is cleaved on the carboxyl side of a proline residue. C) a serine residue serves as the nucleophile during the catalytic event. D) inhibitors have been designed to covalently link to the active site just like natural substrates do. E) None of the above is true. F) All of the above are true.
8. The chemical structure of Coenzyme A contains the following except— a phosphoanhydride moiety. a β-mercaptoethylamine residue. a lipoic acid residue. a pantothenic acid residue. an adenosine-3’- phosphate.
1E In terms of binding adenylate kinase, the Kd for ATP is ~50 M and the KI for GMP-PCP is ~50 nM. Explain how this may be possible in terms of molecular interactions. Name 4 different types of molecular interactions that may contribute to the increased binding affinity exhibited by GMP-PCP. Please help me in details
2. A group of peptides that influence nerve transmission in certain parts of the brain have been isolated from normal brain tissue. These peptides are known as opioids. Using the information below, determine the amino acid sequence of this particular opioid: ● Complete hydrolysis by HCl at 100° C followed by amino acid hydrolysis analysis indicated the presence of Gly, Leu, Phe, and Tyr, in a 2:1:1:1 ratio. ● Treatment of the peptide with FNDB followed by complete hydrolysis indicated the presence of 2,2-dinitrophenyl derivative of tyrosine. No free tyrosine could be found. ● Complete digestion of the peptide with chymotrypsin yielded free tyrosine and leucine, plus a tripeptide containing Phe and Gly in a 1:2 ratio. Instructions Make use of the table below to determine the sequence of the mystery protein:
3CLpro is a cysteine protease, which are among the most common proteases in biochemistry, however they are a structurally diverse family of enzymes especially in the organization of the active site amino acids. A group of scientists have reported a potential drug molecule based on a binding study using circular dichroism. They report that the molecule binds to the active site. Can the experiment support the claims, why or why not? Which techniques might be used to support this claim?